There are various approaches that can be used to fabricate protein polymeric materials. One approach involves modifying the primary structure or nanostructure of a protein using mutagenesis or a suitable genetic engineering means. The changes in the nanostructure of the protein can ultimately affect protein folding and assembly. For example, crosslinkers may be added to the nanostructure of a protein such that random covalent bridges are formed between adjacent parts of the protein to form a polymeric matrix. Another approach involves modifying the assembling process of the macrostructure of a protein to improve the cohesiveness and strength of the protein polymers. Proteins that have been the targets for macrostructure manipulation include those that are capable of self assembling. For example, Collagen has been known to self assemble to form a protein scaffold that can be used to structurally support cell or tissue proliferation, and various techniques for fabricating Collagen scaffolds have been disclosed. However, the known techniques for assembling collagen scaffolds typically yield scaffolds that are composed of randomly arranged fibers. These scaffolds may lack desirable characteristics, such as fiber strength. These characteristics are important, especially in biomedical applications.
Therefore, there is a need to control the process of protein assembly in a manner that provides for an arrangement of protein fibers that promotes the structural strength of the protein matrixes or the scaffolds. There is also a need for strong protein polymers that can be used to support cell or tissue proliferation and regeneration.